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Q9UBB5

- MBD2_HUMAN

UniProt

Q9UBB5 - MBD2_HUMAN

Protein

Methyl-CpG-binding domain protein 2

Gene

MBD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binds hemimethylated DNA as well. Recruits histone deacetylases and DNA methyltransferases. Acts as transcriptional repressor and plays a role in gene silencing. Functions as a scaffold protein, targeting GATAD2A and GATAD2B to chromatin to promote repression. May enhance the activation of some unmethylated cAMP-responsive promoters.6 Publications

    GO - Molecular functioni

    1. C2H2 zinc finger domain binding Source: UniProtKB
    2. chromatin binding Source: Ensembl
    3. methyl-CpG binding Source: UniProtKB
    4. mRNA binding Source: Ensembl
    5. protein binding Source: UniProtKB
    6. protein domain specific binding Source: UniProtKB
    7. satellite DNA binding Source: ProtInc
    8. siRNA binding Source: Ensembl

    GO - Biological processi

    1. ATP-dependent chromatin remodeling Source: UniProt
    2. cellular protein complex assembly Source: Ensembl
    3. maternal behavior Source: Ensembl
    4. negative regulation of transcription, DNA-templated Source: UniProtKB
    5. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. positive regulation of Wnt signaling pathway Source: Ensembl
    7. regulation of cell proliferation Source: Ensembl
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2232. RNA Polymerase I Promoter Opening.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methyl-CpG-binding domain protein 2
    Alternative name(s):
    Demethylase
    Short name:
    DMTase
    Methyl-CpG-binding protein MBD2
    Gene namesi
    Name:MBD2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:6917. MBD2.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Nuclear, in discrete foci. Detected at replication foci in late S phase.

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. heterochromatin Source: Ensembl
    3. histone deacetylase complex Source: Ensembl
    4. nuclear chromatin Source: UniProt
    5. nucleus Source: UniProtKB
    6. protein complex Source: UniProt

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30660.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 411411Methyl-CpG-binding domain protein 2PRO_0000096260Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei181 – 1811Phosphoserine2 Publications
    Modified residuei407 – 4071Phosphoserine4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UBB5.
    PaxDbiQ9UBB5.
    PRIDEiQ9UBB5.

    PTM databases

    PhosphoSiteiQ9UBB5.

    Expressioni

    Tissue specificityi

    Highly expressed in brain, heart, kidney, stomach, testis and placenta.1 Publication

    Gene expression databases

    ArrayExpressiQ9UBB5.
    BgeeiQ9UBB5.
    CleanExiHS_MBD2.
    GenevestigatoriQ9UBB5.

    Organism-specific databases

    HPAiCAB037282.

    Interactioni

    Subunit structurei

    Heterodimer with MBD3. Component of the MeCP1 complex that contains HDAC1 and HDAC2. Binds DNMT1, MIZF, GPN1, SIN3A, GATAD2A/p66-alpha and GATAD2B/p66-beta. Interacts with DHX9.10 Publications

    Protein-protein interaction databases

    BioGridi114445. 34 interactions.
    IntActiQ9UBB5. 5 interactions.
    MINTiMINT-210249.
    STRINGi9606.ENSP00000256429.

    Structurei

    Secondary structure

    1
    411
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi366 – 38823
    Turni389 – 3924

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L2LNMR-B360-393[»]
    ProteinModelPortaliQ9UBB5.
    SMRiQ9UBB5. Positions 149-213, 360-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini145 – 21369MBDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 149149Necessary for interaction with DHX9Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi6 – 140135Gly-richAdd
    BLAST
    Compositional biasi50 – 9647Arg-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 MBD (methyl-CpG-binding) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG316386.
    HOGENOMiHOG000013073.
    HOVERGENiHBG052417.
    InParanoidiQ9UBB5.
    KOiK11590.
    OMAiNCISICC.
    OrthoDBiEOG7QNVMV.
    PhylomeDBiQ9UBB5.
    TreeFamiTF325032.

    Family and domain databases

    Gene3Di3.30.890.10. 2 hits.
    InterProiIPR016177. DNA-bd_dom.
    IPR025884. MeCpG-bd_2/3_C_dom.
    IPR001739. Methyl_CpG_DNA-bd.
    [Graphical view]
    PfamiPF01429. MBD. 1 hit.
    PF14048. MBD_C. 1 hit.
    [Graphical view]
    SMARTiSM00391. MBD. 1 hit.
    [Graphical view]
    SUPFAMiSSF54171. SSF54171. 1 hit.
    PROSITEiPS50982. MBD. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UBB5-1) [UniParc]FASTAAdd to Basket

    Also known as: MBD2a, MBD2b

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRAHPGGGRC CPEQEEGESA AGGSGAGGDS AIEQGGQGSA LAPSPVSGVR    50
    REGARGGGRG RGRWKQAGRG GGVCGRGRGR GRGRGRGRGR GRGRGRPPSG 100
    GSGLGGDGGG CGGGGSGGGG APRREPVPFP SGSAGPGPRG PRATESGKRM 150
    DCPALPPGWK KEEVIRKSGL SAGKSDVYYF SPSGKKFRSK PQLARYLGNT 200
    VDLSSFDFRT GKMMPSKLQK NKQRLRNDPL NQNKGKPDLN TTLPIRQTAS 250
    IFKQPVTKVT NHPSNKVKSD PQRMNEQPRQ LFWEKRLQGL SASDVTEQII 300
    KTMELPKGLQ GVGPGSNDET LLSAVASALH TSSAPITGQV SAAVEKNPAV 350
    WLNTSQPLCK AFIVTDEDIR KQEERVQQVR KKLEEALMAD ILSRAADTEE 400
    MDIEMDSGDE A 411
    Length:411
    Mass (Da):43,255
    Last modified:May 1, 2000 - v1
    Checksum:iFC4E5E0CF9BA0FFA
    GO
    Isoform 3 (identifier: Q9UBB5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         235-302: GKPDLNTTLP...SDVTEQIIKT → LRWNTHRPAP...YSRQNQSFPP
         303-411: Missing.

    Note: Incomplete sequence.

    Show »
    Length:302
    Mass (Da):31,745
    Checksum:iCCEC65D926222717
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei235 – 30268GKPDL…QIIKT → LRWNTHRPAPWHALSRLCLL IRCLLCLECAYPLPLHLVNS YSSKTQLHCLHLWEACPAYS RQNQSFPP in isoform 3. 1 PublicationVSP_011077Add
    BLAST
    Alternative sequencei303 – 411109Missing in isoform 3. 1 PublicationVSP_011078Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072242 mRNA. Translation: AAC68871.1.
    AF072246 mRNA. Translation: AAC68875.1.
    AF120989, AF120988 Genomic DNA. Translation: AAD56596.1.
    AF120993
    , AF120988, AF120989, AF120990, AF120991, AF120992 Genomic DNA. Translation: AAD56597.1.
    BC032638 mRNA. Translation: AAH32638.1.
    CCDSiCCDS11953.1. [Q9UBB5-1]
    CCDS45871.1. [Q9UBB5-3]
    RefSeqiNP_003918.1. NM_003927.4. [Q9UBB5-1]
    NP_056647.1. NM_015832.4. [Q9UBB5-3]
    UniGeneiHs.25674.

    Genome annotation databases

    EnsembliENST00000256429; ENSP00000256429; ENSG00000134046. [Q9UBB5-1]
    ENST00000583046; ENSP00000464554; ENSG00000134046. [Q9UBB5-3]
    GeneIDi8932.
    KEGGihsa:8932.
    UCSCiuc002lfg.2. human. [Q9UBB5-1]
    uc002lfh.2. human. [Q9UBB5-3]

    Polymorphism databases

    DMDMi50401198.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072242 mRNA. Translation: AAC68871.1 .
    AF072246 mRNA. Translation: AAC68875.1 .
    AF120989 , AF120988 Genomic DNA. Translation: AAD56596.1 .
    AF120993
    , AF120988 , AF120989 , AF120990 , AF120991 , AF120992 Genomic DNA. Translation: AAD56597.1 .
    BC032638 mRNA. Translation: AAH32638.1 .
    CCDSi CCDS11953.1. [Q9UBB5-1 ]
    CCDS45871.1. [Q9UBB5-3 ]
    RefSeqi NP_003918.1. NM_003927.4. [Q9UBB5-1 ]
    NP_056647.1. NM_015832.4. [Q9UBB5-3 ]
    UniGenei Hs.25674.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L2L NMR - B 360-393 [» ]
    ProteinModelPortali Q9UBB5.
    SMRi Q9UBB5. Positions 149-213, 360-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114445. 34 interactions.
    IntActi Q9UBB5. 5 interactions.
    MINTi MINT-210249.
    STRINGi 9606.ENSP00000256429.

    Chemistry

    DrugBanki DB01355. Hexobarbital.

    PTM databases

    PhosphoSitei Q9UBB5.

    Polymorphism databases

    DMDMi 50401198.

    Proteomic databases

    MaxQBi Q9UBB5.
    PaxDbi Q9UBB5.
    PRIDEi Q9UBB5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256429 ; ENSP00000256429 ; ENSG00000134046 . [Q9UBB5-1 ]
    ENST00000583046 ; ENSP00000464554 ; ENSG00000134046 . [Q9UBB5-3 ]
    GeneIDi 8932.
    KEGGi hsa:8932.
    UCSCi uc002lfg.2. human. [Q9UBB5-1 ]
    uc002lfh.2. human. [Q9UBB5-3 ]

    Organism-specific databases

    CTDi 8932.
    GeneCardsi GC18M051615.
    HGNCi HGNC:6917. MBD2.
    HPAi CAB037282.
    MIMi 603547. gene.
    neXtProti NX_Q9UBB5.
    PharmGKBi PA30660.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG316386.
    HOGENOMi HOG000013073.
    HOVERGENi HBG052417.
    InParanoidi Q9UBB5.
    KOi K11590.
    OMAi NCISICC.
    OrthoDBi EOG7QNVMV.
    PhylomeDBi Q9UBB5.
    TreeFami TF325032.

    Enzyme and pathway databases

    Reactomei REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2232. RNA Polymerase I Promoter Opening.

    Miscellaneous databases

    ChiTaRSi MBD2. human.
    GeneWikii Methyl-CpG-binding_domain_protein_2.
    GenomeRNAii 8932.
    NextBioi 33582.
    PROi Q9UBB5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBB5.
    Bgeei Q9UBB5.
    CleanExi HS_MBD2.
    Genevestigatori Q9UBB5.

    Family and domain databases

    Gene3Di 3.30.890.10. 2 hits.
    InterProi IPR016177. DNA-bd_dom.
    IPR025884. MeCpG-bd_2/3_C_dom.
    IPR001739. Methyl_CpG_DNA-bd.
    [Graphical view ]
    Pfami PF01429. MBD. 1 hit.
    PF14048. MBD_C. 1 hit.
    [Graphical view ]
    SMARTi SM00391. MBD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54171. SSF54171. 1 hit.
    PROSITEi PS50982. MBD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a family of mammalian methyl-CpG binding proteins."
      Hendrich B., Bird A.
      Mol. Cell. Biol. 18:6538-6547(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 157-411 (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Testis.
    2. "Genomic structure and chromosomal mapping of the murine and human mbd1, mbd2, mbd3, and mbd4 genes."
      Hendrich B., Abbott C., McQueen H., Chambers D., Cross S.H., Bird A.
      Mamm. Genome 10:906-912(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lymph.
    4. "A mammalian protein with specific demethylase activity for mCpG DNA."
      Bhattacharya S.K., Ramchandani S., Cervoni N., Szyf M.
      Nature 397:579-583(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 1), TISSUE SPECIFICITY.
    5. "MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex."
      Ng H.-H., Zhang Y., Hendrich B., Johnson C.A., Turner B.M., Erdjument-Bromage H., Tempst P., Reinberg D., Bird A.
      Nat. Genet. 23:58-61(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MECP1 AND HDAC1.
    6. "MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase."
      Tatematsu K., Yamazaki T., Ishikawa F.
      Genes Cells 5:677-688(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HETERODIMERIZATION WITH MBD3, INTERACTION WITH DNMT1.
    7. "The minimal repression domain of MBD2b overlaps with the methyl-CpG-binding domain and binds directly to Sin3A."
      Boeke J., Ammerpohl O., Kegel S., Moehren U., Renkawitz R.
      J. Biol. Chem. 275:34963-34967(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 1), INTERACTION WITH SIN3A.
    8. "Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1."
      Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y., Howard B.H.
      J. Biol. Chem. 276:6817-6824(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC1, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Involvement of a novel zinc finger protein, MIZF, in transcriptional repression by interacting with a methyl-CpG-binding protein, MBD2."
      Sekimata M., Takahashi A., Murakami-Sekimata A., Homma Y.
      J. Biol. Chem. 276:42632-42638(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MIZF.
    10. "Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3."
      Brackertz M., Boeke J., Zhang R., Renkawitz R.
      J. Biol. Chem. 277:40958-40966(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH P66ALPHA AND P66BETA, SUBCELLULAR LOCATION.
    11. "MBDin, a novel MBD2-interacting protein, relieves MBD2 repression potential and reactivates transcription from methylated promoters."
      Lembo F., Pero R., Angrisano T., Vitiello C., Iuliano R., Bruni C.B., Chiariotti L.
      Mol. Cell. Biol. 23:1656-1665(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GPN1.
    12. Cited for: FUNCTION, INTERACTION WITH DHX9.
    13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "p66alpha and p66beta of the Mi-2/NuRD complex mediate MBD2 and histone interaction."
      Brackertz M., Gong Z., Leers J., Renkawitz R.
      Nucleic Acids Res. 34:397-406(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GATAD2A AND GATAD2B.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Probing the dynamic distribution of bound states for methylcytosine-binding domains on DNA."
      Cramer J.M., Scarsdale J.N., Walavalkar N.M., Buchwald W.A., Ginder G.D., Williams D.C. Jr.
      J. Biol. Chem. 289:1294-1302(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING.
    21. "p66Alpha-MBD2 coiled-coil interaction and recruitment of Mi-2 are critical for globin gene silencing by the MBD2-NuRD complex."
      Gnanapragasam M.N., Scarsdale J.N., Amaya M.L., Webb H.D., Desai M.A., Walavalkar N.M., Wang S.Z., Zu Zhu S., Ginder G.D., Williams D.C. Jr.
      Proc. Natl. Acad. Sci. U.S.A. 108:7487-7492(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 360-393 IN COMPLEX WITH GATAD2A, SUBUNIT, INTERACTION WITH GATAD2A.

    Entry informationi

    Entry nameiMBD2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBB5
    Secondary accession number(s): O95242, Q9UIS8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3